Evidence map›Paper›PMID 19038269›Full record

ArticleJournal of molecular biology2009

Activity and specificity of the bacterial PD-(D/E)XK homing endonuclease I-Ssp6803I.

Lei Zhao, Stefan Pellenz, Barry L Stoddard

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.9field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Rapid determination of homing endonuclease DNA binding specificity profile.Methods in molecular biology (Clifton, N.J.) · 2014
    Article
  5. Homing endonucleases: from genetic anomalies to programmable genomic clippers.Methods in molecular biology (Clifton, N.J.) · 2014
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Homing endonucleases: from basics to therapeutic applications.Cellular and molecular life sciences : CMLS · 2010
    Review
  11. Article
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Lei ZhaoGraduate Program in Molecular Biophysics, Structure and Design, University of Washington, Seattle, WA 98195, USA.
Stefan Pellenz
Barry L Stoddard
University of Washington · USFred Hutch Cancer Center · US

Funding

Structure, function &engineering of nuclease catalystsR01GM049857 · NIGMS · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 1994 to 2014
$4.2M
Structural and Biophysical Characterization of Engineered Homing Endonucleases (CRL1CA133833 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI STODDARD, BARRY L. · 2007 to 2011
$2.1M
NCI NIH HHS RL1 CA133833NIGMS NIH HHS R01 GM049857NIGMS NIH HHS R01 GM49857
6 · The paper itself

Abstract

The restriction endonuclease fold [a three-layer alpha-beta sandwich containing variations of the PD-(D/E)XK nuclease motif] has been greatly diversified during evolution, facilitating its use for many biological functions. Here we characterize DNA binding and cleavage by the PD-(D/E)XK homing endonuclease I-Ssp6803I. Unlike most restriction endonucleases harboring the same core fold, the specificity profile of this enzyme extends over a long (17 bp) target site. The DNA binding and cleavage specificity profiles of this enzyme were independently determined and found to be highly correlated. However, the DNA target sequence contains several positions where binding and cleavage activities are not tightly coupled: individual DNA base-pair substitutions at those positions that significantly decrease cleavage activity have minor effects on binding affinity. These changes in the DNA target sequence appear to correspond to substitutions that uniquely increase the free energy change between the ground state and the transition state, rather than simply decreasing the overall DNA binding affinity. The specificity of the enzyme reflects constraints on its host gene and limitations imposed by the enzyme's quaternary structure and illustrate the highly diverse repertoire of DNA recognition specificities that can be adopted by the related folds surrounding the PD-(D/E)XK nuclease motif.

Indexed as

Models, MolecularAmino Acid SequenceBacterial ProteinsDNA, BacterialDNA Restriction EnzymesMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingProtein FoldingProtein Structure, QuaternaryProtein Structure, SecondarySynechocystisBacterial ProteinsDNA, BacterialDNA Restriction Enzymes

Identifiers

PMID19038269
PMCPMC3008403
OpenAlexW1980258351

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.